Microwave-assisted solid-phase synthesis of lactosylated peptides for food analytical application.

The lactosylation of whey proteins affects their properties, especially their allergenicity and nutritional value, which matters in infant feeding. The quantification of lactosylated peptides requires analytically pure standards which are not commercially available. Herein, we proposed a fast, simple, and efficient protocol for the synthesis of lactosylated peptides on solid support based on microwave-assisted synthesis combined with boronate affinity chromatography utilizing the functionalized resin developed in our research group.

High-Temperature, Solid-Phase Reaction of α-Amino Groups in Peptides with Lactose and Glucose: An Alternative Mechanism Leading to an α-Ketoacyl Derivative.

The reaction of proteins with reducing sugars results in the formation of Amadori products, which involves the N-terminal group and/or ε-amino group of the lysine side chain. However, less attention has been given to the reactivity of the N-terminus of a peptide chain under similar conditions. In our work, we focused on the reaction of the α-amino group of peptides in the presence of a reducing sugar, specifically lactose.

HPLC-free method of synthesis of isotopically labeled deoxyfructosylated peptides.

The biomarker strategy, based on multiple specific glycation sites in plasma proteins, could essentially increase the efficiency of glycemic control and disease prediction. Besides glycated albumin being a potential biomarker of early states of diabetes mellitus and control of short-term, it has been shown that the glycation of fibrinogen may also impact the formation of the fibrin network, while quantification of glycation of the CD59 protein allows for early detection of glucose intolerance in pregnant women. A different level of glycation of individual lysine residues in proteins has a crucial influence on the stages of the disease.